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2000 | 47 | 2 |

Tytuł artykułu

The participation of ribosome-UDP-GalNAc complex in the initiation of protein glycosylation in vitro

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The gastric epithelial cells ribosome-UDP-GalNAc complex is a donor of UDP- GalNAc as the substrate for N-acetylgalactosaminyltransferase, which catalyse the transfer of GalNAc residue to the polypeptide, existing on polysomes. It was observed that the deglycosylated porcine mucin and synthetic peptide (PTSSPIST) can be also glycosylated with participation of N-acetylgalactosaminyltransferase and ribosome- UDP-GalNAc complex. The probability of the ribosome-UDP-GalNAc complex as an intermediate in the O-glycosylation is considered.

Wydawca

-

Rocznik

Tom

47

Numer

2

Opis fizyczny

p.421-426

Twórcy

  • Medical Academy, 15-230 Bialystok 8, Poland
autor

Bibliografia

  • 1. Abeijon, C. & Hirschberg, C.B. (1987) Subcellular site of synthesis of the ^-acetylgalactosamine (alphal-O) serine (or threonine) linkage in rat liver. J. Biol. Chem. 262, 4153-4159.
  • 2. Elhammer, A. & Kornfeld, S. (1984) Two enzymes involved in the synthesis of O-linked oligosaccharides are localized on membranes of different densities in mouse lymphoma BW5147 cells. J. Cell Biol. 98, 327-331.
  • 3. Piller, V., Piller, F. & Fukuda, M. (1990) Biosynthesis of truncated O-glycans in the T cell line Jurkat. Localization of O-glycan initiation. J. Biol. Chem. 265, 9264-9271.
  • 4. Roth, J., Wang, Y., Eckhardt, A.E. & Hill, R.L. (1994) Subcellular localization of the UDP-N- acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland. Proc. Natl. Acad. Sci. U.S.A. 91, 8935-8939.
  • 5. Sweizer, A., Clausen, H., van Meer, G. & Hauri, H.P. (1994) Localization of glycans initiation, sphingomyelin synthesis, and glycosylceramide synthesis in Vero cells with respect to the endoplasmic reticulum Golgi intermediate compartment. J. Biol. Chem. 269, 4035-4041.
  • 6. Palzelt, C. & Weber, B. (1986) Early O-glycosidic glycosylation of proglucagon in pancreatic islets: An unusual type of prohormonal modification. EMBO J. 5, 2103-2108.
  • 7. Perez-Vilar, J., Hidalgo, J. & Velasco, A. (1991) Presence of terminal N-acetylgalactosamine residues in subregions of the endoplasmic reticulum is influenced by cell differentiation in culture. J. Biol. Chem. 266, 23967-23976.
  • 8. Ellinger, A. & Pavelka, M. (1992) Subdomains of rough endoplasmic reticulum in colon goblet cells of the rat: Lectin-cytochemical characterization. J. Histochem. Cytochem. 40, 919-930.
  • 9. Kopacz-Jodczyk, T. & Galasinski, W. (1987) The binding of decomposition products of UDP-galactose to the microsomes and polyribosomes isolated from rat liver. Biochem. Med. Metab. Biol. 38, 149-155.
  • 10. Kopacz-Jodczyk, T., Paszkiewicz-Gadek, A. & Galasinski, W. (1988) The attachment of UDP-hexosamines to the ribosomes isolated from rat liver. Biochem. Med. Metab. Biol. 39, 290-295.
  • 11. Paszkiewicz-Gadek, A., Gindzienski, A. & Porowska, H. (1996) Nucleotide-sugar binding to ribosomes. Comparison of affinity and capacity of gastric mucosa and liver ribosomes to sugar-nucleotides. Ann. Acad. Med. Bialostocensis41, 305-315.
  • 12. Paszkiewicz-Gadek, A., Porowska, H. & Galasinski, W. (1992) The participation of ribosomes in protein glycosylation. Interaction of the ribosome-UDP-N-acetylglucosamine complex with dolichol phosphate. Acta Biochim. Polon. 39, 251-264.
  • 13. Jablonowska, K., Kopacz-Jodczyk, T., Niedzwiecka, J. & Galasinski, W. (1983) Isolation and characterization of elongation factor EF-2 from Guerin tumour. Acta Biochim. Polon. 30, 381-389.
  • 14. Petermann, M.L. (1964) The Physical and Chemical Properties of Ribosomes; pp. 63, American Elsevier, New York.
  • 15. Lowry, O.H., Rosebrough, N.J., Farr, A.L. & Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275.
  • 16. Leder, P. & Bursztyn, H. (1966) Initiation of protein synthesis. II. A convenient assay for the ribosome-dependent synthesis of N-formyl-14C-metionyl-puromycin. Biochem. Biophys. Res. Commun. 25, 233-238.
  • 17. Gindzienski, A. & Zwierz, K. (1987) Isolation and fractionation of human gastric mucus gel. Biomed. Biochim. Acta 46, 165-176.
  • 18. Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A. & Smith, F. (1956) The phenol- sulfuric acid reaction for carbohydrates. Anal. Chem. 28, 350-356.
  • 19. Thornton, D.J., Howard, M., Devine, P.L. & Sheehan, J.K. (1995) Methods for separation and deglycosylation of mucin subunits. Anal. Biochem. 227, 162-167.
  • 20. Raju, T.S. & Davidson, E.A. (1994) New approach towards deglycosylation of sialoglycoproteins and mucins. Biochem. Mol. Biol. Int. 34, 943-954.
  • 21. Gerken, J.A., Gupta, R. & Jentoft, N. (1992) A novel approach for chemically deglycosylating O-linked glycoproteins. The deglycosylation of submaxillary and respiratory mucins. Biochemistry 31, 639-648.
  • 22. Porowska, H., Paszkiewicz-Gadek, A., Gindzienski, A. (1999) Activity of partially purified UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase with different peptide acceptors. Acta Biochim. Polon. 46, 365-370.
  • 23. Wang, Y., Abemethy, J.L, Eckhardt, A.E. & Hill, R.L. (1992) Purification and characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase specific for glycosylation of treonine residues. J. Biol. Chem. 267, 12709-12716.
  • 24. Mendicino, J. & Sangadala, S. (1998) Purification and charcterization of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase from swine trachea epithelium. Mol. Cell. Biochem. 185, 135-145.
  • 25. Gerken, T.A., Owens, C.L. & Pasumarthy, M. (1998) Site-specific core 1-O-glycosylation pattern of the porcine submaxillary gland mucin tandem repeat. Evidence for the modulation of glycan length by peptide sequence. J. Biol. Chem. 273, 26580-26588.

Typ dokumentu

Bibliografia

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Identyfikator YADDA

bwmeta1.element.agro-article-d981a1de-fc75-41b0-923a-e66ff551f4ff
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